It is now evident that cell surface glycoconjugates play a central role in mediating the social responses of cells and may have specific effector functions associated with the carbohydrate moiety of these molecules. We propose to determine the structure of the carbohydrate moieties of the murine histocompatibility H-2K and D antigens and relate this to the serotype of these glycoproteins. To accomplish this we will employ sensitive serological and immunochemical techniques to perform partial sequence analysis of membrane bound H-2K and D antigens. In addition, a novel electrophoretic biochemical method will be used to obtain the carbohydrate sequence of the glycopeptides derived from immuno-purified H-2K and D antigens. The reliability and versatility of the polyacrylamide gel electrophoretic procedure for the structural analysis of glycopeptides will be demonstrated using various glycopeptides of known structure and employing methylation analysis of the glycopeptides. These studies will assess the possibility of a mechanism which controls and/or links the processes responsible for the biosynthesis of the carbohydrate and polypeptide portions of glycoproteins.